Glycobiology Advance Access originally published online on October 9, 2003
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Glycobiology vol 14 no 2 pp. 139-146, 2004
© Oxford University Press 2004; all rights reserved.
Addition of ß1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin
2 Department of Biochemistry, Osaka University Graduate School of Medicine, B1, 2-2, Yamadaoka, Suita, Osaka 565-0871, Japan; 3 Department of Molecular Biochemistry and Clinical Investigations, Osaka University University Graduate School of Medicine, 1-7 Yamadaoka, Suita, Osaka 565-0871, Japan; and 4 Department of Oncology, Lombardi Cancer Center, Georgetown University, Medical Center, Washington, DC 20007
Received on June 25, 2003; revised on September 26, 2003; accepted on September 29, 2003
ß1-6 GlcNAc branching, a product of N-acetylglucosaminyltransferase V (GnT-V), is a key structure that is associated with malignant transformations and cancer metastasis. Although a number of reports concerning tumor metastasis–related glycoproteins that contain ß1-6 GlcNAc branching have appeared, the precise function of ß1-6 GlcNAc branching on glycoproteins remains to be elucidated. We previously reported on the importance of ß1-6 GlcNAc branching on matriptase in terms of proteolytic degradation in tumor metastasis. We report here that matriptase purified from GnT-V transfectant (ß1-6 GlcNAc matriptase) binds strongly to L4-PHA, which preferentially recognizes ß1-6 GlcNAc branches of tri- or tetraantennary sugar chains, indicating that the isolated matriptase contains ß1-6 GlcNAc branching. The ß1-6 GlcNAc matriptase was resistant to autodegradation, as well as trypsin digestion, compared with matriptase purified from mock-transfected cells. Furthermore, N-glycosidase-F treatment of ß1-6 GlcNAc matriptase greatly reduced its resistance to degradation. An analysis of matriptase mutants that do not contain potential N-glycosylation sites clearly shows that the ß1-6 GlcNAc branching on N-glycans attached to Asn 772 in the serine protease domain plays a major role in trypsin resistance. This is the first example of a demonstration of a direct relationship between ß1-6 GlcNAc branching and a biological function at the protein level.
1 To whom correspondence should be addressed; e-mail: seika{at}biochem.med.osaka-u.ac.jp
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